ID Q8E1F5_STRA5 Unreviewed; 168 AA.
AC Q8E1F5;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=tRNA-specific adenosine deaminase {ECO:0000256|HAMAP-Rule:MF_00972};
DE EC=3.5.4.33 {ECO:0000256|HAMAP-Rule:MF_00972};
GN Name=tadA {ECO:0000256|HAMAP-Rule:MF_00972};
GN OrderedLocusNames=SAG0400 {ECO:0000313|EMBL:AAM99306.1};
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435 {ECO:0000313|EMBL:AAM99306.1, ECO:0000313|Proteomes:UP000000821};
RN [1] {ECO:0000313|EMBL:AAM99306.1, ECO:0000313|Proteomes:UP000000821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821};
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin S., Kolonay J.F., Umayam L.A., Madupu R., Lewis M.R.,
RA Radune D., Fedorova N.B., Scanlan D., Khouri H., Mulligan S., Carty H.A.,
RA Cline R.T., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C.,
RA Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R.,
RA Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC -!- FUNCTION: Catalyzes the deamination of adenosine to inosine at the
CC wobble position 34 of tRNA(Arg2). {ECO:0000256|HAMAP-Rule:MF_00972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC Evidence={ECO:0000256|ARBA:ARBA00001103, ECO:0000256|HAMAP-
CC Rule:MF_00972};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00972};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00972};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00972}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT2 subfamily. {ECO:0000256|ARBA:ARBA00010669}.
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DR EMBL; AE009948; AAM99306.1; -; Genomic_DNA.
DR RefSeq; NP_687434.1; NC_004116.1.
DR RefSeq; WP_001169006.1; NC_004116.1.
DR AlphaFoldDB; Q8E1F5; -.
DR STRING; 208435.SAG0400; -.
DR GeneID; 66885375; -.
DR KEGG; sag:SAG0400; -.
DR PATRIC; fig|208435.3.peg.395; -.
DR HOGENOM; CLU_025810_3_2_9; -.
DR OrthoDB; 9802676at2; -.
DR Proteomes; UP000000821; Chromosome.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:UniProtKB-UniRule.
DR CDD; cd01285; nucleoside_deaminase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR028883; tRNA_aden_deaminase.
DR PANTHER; PTHR11079:SF179; CYTOSINE DEAMINASE; 1.
DR PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR Pfam; PF14437; MafB19-deam; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00972};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00972}; Reference proteome {ECO:0000313|Proteomes:UP000000821};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00972};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00972}.
FT DOMAIN 7..134
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 60
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
SQ SEQUENCE 168 AA; 18991 MW; 30B622911DB4D722 CRC64;
MQKFTQEEKE WFMTEALKEA KSSLEKEEIP IGCVIVKDGH IIGRGHNARE EFNKAILHAE
IMAINNANEK VGNWRLLDTT LFVTVEPCVM CSGAIGLARI PHVIYGAKNT KFGAAGSLYD
ILSDSRLNHR VEVETGILED QCAKIMQDFF RKGRQRKKEA KLSEKTKI
//
